Arabidopsis At5g39790 encodes a chloroplast-localized, carbohydrate-binding, coiled-coil domain-containing putative scaffold protein
Identifieur interne : 000921 ( Ncbi/Merge ); précédent : 000920; suivant : 000922Arabidopsis At5g39790 encodes a chloroplast-localized, carbohydrate-binding, coiled-coil domain-containing putative scaffold protein
Auteurs : Elke M. Lohmeier-Vogel [Canada] ; David Kerk [Canada] ; Mhairi Nimick [Canada] ; Susan Wrobel [Canada] ; Lori Vickerman [Canada] ; Douglas G. Muench [Canada] ; Greg Bg Moorhead [Canada]Source :
- BMC Plant Biology [ 1471-2229 ] ; 2008.
Abstract
Starch accumulation and degradation in chloroplasts is accomplished by a suite of over 30 enzymes. Recent work has emphasized the importance of multi-protein complexes amongst the metabolic enzymes, and the action of associated non-enzymatic regulatory proteins. Arabidopsis At5g39790 encodes a protein of unknown function whose sequence was previously demonstrated to contain a putative carbohydrate-binding domain.
We here show that At5g39790 is chloroplast-localized, and binds starch, with a preference for amylose. The protein persists in starch binding under conditions of pH, redox and Mg+2 concentrations characteristic of both the day and night chloroplast cycles. Bioinformatic analysis demonstrates a diurnal pattern of gene expression, with an accumulation of transcript during the light cycle and decline during the dark cycle. A corresponding diurnal pattern of change in protein levels in leaves is also observed. Sequence analysis shows that At5g39790 has a strongly-predicted coiled-coil domain. Similar analysis of the set of starch metabolic enzymes shows that several have strong to moderate coiled-coil potential. Gene expression analysis shows strongly correlated patterns of co-expression between At5g39790 and several starch metabolic enzymes.
We propose that At5g39790 is a regulatory scaffold protein, persistently binding the starch granule, where it is positioned to interact by its coiled-coil domain with several potential starch metabolic enzyme binding-partners.
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DOI: 10.1186/1471-2229-8-120
PubMed: 19038037
PubMed Central: 2653042
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Lohmeier-Vogel</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Kerk, David" sort="Kerk, David" uniqKey="Kerk D" first="David" last="Kerk">David Kerk</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Nimick, Mhairi" sort="Nimick, Mhairi" uniqKey="Nimick M" first="Mhairi" last="Nimick">Mhairi Nimick</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Wrobel, Susan" sort="Wrobel, Susan" uniqKey="Wrobel S" first="Susan" last="Wrobel">Susan Wrobel</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Vickerman, Lori" sort="Vickerman, Lori" uniqKey="Vickerman L" first="Lori" last="Vickerman">Lori Vickerman</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Muench, Douglas G" sort="Muench, Douglas G" uniqKey="Muench D" first="Douglas G" last="Muench">Douglas G. 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Lohmeier-Vogel</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Kerk, David" sort="Kerk, David" uniqKey="Kerk D" first="David" last="Kerk">David Kerk</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Nimick, Mhairi" sort="Nimick, Mhairi" uniqKey="Nimick M" first="Mhairi" last="Nimick">Mhairi Nimick</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Wrobel, Susan" sort="Wrobel, Susan" uniqKey="Wrobel S" first="Susan" last="Wrobel">Susan Wrobel</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Vickerman, Lori" sort="Vickerman, Lori" uniqKey="Vickerman L" first="Lori" last="Vickerman">Lori Vickerman</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Muench, Douglas G" sort="Muench, Douglas G" uniqKey="Muench D" first="Douglas G" last="Muench">Douglas G. Muench</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Moorhead, Greg Bg" sort="Moorhead, Greg Bg" uniqKey="Moorhead G" first="Greg Bg" last="Moorhead">Greg Bg Moorhead</name><affiliation wicri:level="4"><nlm:aff id="I1">Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</nlm:aff><orgName type="university">Université de Calgary</orgName><country>Canada</country><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author></analytic><series><title level="j">BMC Plant Biology</title><idno type="eISSN">1471-2229</idno><imprint><date when="2008">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Background</title><p>Starch accumulation and degradation in chloroplasts is accomplished by a suite of over 30 enzymes. Recent work has emphasized the importance of multi-protein complexes amongst the metabolic enzymes, and the action of associated non-enzymatic regulatory proteins. Arabidopsis At5g39790 encodes a protein of unknown function whose sequence was previously demonstrated to contain a putative carbohydrate-binding domain.</p></sec><sec><title>Results</title><p>We here show that At5g39790 is chloroplast-localized, and binds starch, with a preference for amylose. The protein persists in starch binding under conditions of pH, redox and Mg<sup>+2 </sup>concentrations characteristic of both the day and night chloroplast cycles. Bioinformatic analysis demonstrates a diurnal pattern of gene expression, with an accumulation of transcript during the light cycle and decline during the dark cycle. A corresponding diurnal pattern of change in protein levels in leaves is also observed. Sequence analysis shows that At5g39790 has a strongly-predicted coiled-coil domain. Similar analysis of the set of starch metabolic enzymes shows that several have strong to moderate coiled-coil potential. Gene expression analysis shows strongly correlated patterns of co-expression between At5g39790 and several starch metabolic enzymes.</p></sec><sec><title>Conclusion</title><p>We propose that At5g39790 is a regulatory scaffold protein, persistently binding the starch granule, where it is positioned to interact by its coiled-coil domain with several potential starch metabolic enzyme binding-partners.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct></listBibl></div1></back></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">BMC Plant Biol</journal-id><journal-title>BMC Plant Biology</journal-title><issn pub-type="epub">1471-2229</issn><publisher><publisher-name>BioMed Central</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">19038037</article-id><article-id pub-id-type="pmc">2653042</article-id><article-id pub-id-type="publisher-id">1471-2229-8-120</article-id><article-id pub-id-type="doi">10.1186/1471-2229-8-120</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Arabidopsis At5g39790 encodes a chloroplast-localized, carbohydrate-binding, coiled-coil domain-containing putative scaffold protein</article-title></title-group><contrib-group><contrib id="A1" equal-contrib="yes" contrib-type="author"><name><surname>Lohmeier-Vogel</surname><given-names>Elke M</given-names></name><xref ref-type="aff" rid="I1">1</xref><email>lohmeier@ucalgary.ca</email></contrib><contrib id="A2" equal-contrib="yes" contrib-type="author"><name><surname>Kerk</surname><given-names>David</given-names></name><xref ref-type="aff" rid="I1">1</xref><email>DavidKerk@pointloma.edu</email></contrib><contrib id="A3" contrib-type="author"><name><surname>Nimick</surname><given-names>Mhairi</given-names></name><xref ref-type="aff" rid="I1">1</xref><email>mnimick@ucalgary.ca</email></contrib><contrib id="A4" contrib-type="author"><name><surname>Wrobel</surname><given-names>Susan</given-names></name><xref ref-type="aff" rid="I1">1</xref><email>sawrobel@gmail.com</email></contrib><contrib id="A5" contrib-type="author"><name><surname>Vickerman</surname><given-names>Lori</given-names></name><xref ref-type="aff" rid="I1">1</xref><email>lvickerman@ucalgary.ca</email></contrib><contrib id="A6" contrib-type="author"><name><surname>Muench</surname><given-names>Douglas G</given-names></name><xref ref-type="aff" rid="I1">1</xref><email>dmuench@ucalgary.ca</email></contrib><contrib id="A7" corresp="yes" contrib-type="author"><name><surname>Moorhead</surname><given-names>Greg BG</given-names></name><xref ref-type="aff" rid="I1">1</xref><email>Moorhead@ucalgary.ca</email></contrib></contrib-group><aff id="I1"><label>1</label>Department of Biological Sciences and Alberta Ingenuity Center for Carbohydrate Science, University of Calgary, Calgary, Alberta, Canada, T2N 1N4</aff><pub-date pub-type="collection"><year>2008</year></pub-date><pub-date pub-type="epub"><day>27</day><month>11</month><year>2008</year></pub-date><volume>8</volume><fpage>120</fpage><lpage>120</lpage><ext-link ext-link-type="uri" xlink:href="http://www.biomedcentral.com/1471-2229/8/120"></ext-link><history><date date-type="received"><day>27</day><month>8</month><year>2008</year></date><date date-type="accepted"><day>27</day><month>11</month><year>2008</year></date></history><permissions><copyright-statement>Copyright © 2008 Lohmeier-Vogel et al; licensee BioMed Central Ltd.</copyright-statement><copyright-year>2008</copyright-year><copyright-holder>Lohmeier-Vogel et al; licensee BioMed Central Ltd.</copyright-holder><license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/2.0"><p>This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/2.0"></ext-link>), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</p><pmc-comment>
Lohmeier-Vogel
M
Elke
lohmeier@ucalgary.ca
Arabidopsis At5g39790 encodes a chloroplast-localized, carbohydrate-binding, coiled-coil domain-containing putative scaffold protein
2008 BMC Plant Biology 8(1): 120-. (2008) 1471-2229(2008)8:1<120> urn:ISSN:1471-2229
</license></permissions><abstract><sec><title>Background</title><p>Starch accumulation and degradation in chloroplasts is accomplished by a suite of over 30 enzymes. Recent work has emphasized the importance of multi-protein complexes amongst the metabolic enzymes, and the action of associated non-enzymatic regulatory proteins. Arabidopsis At5g39790 encodes a protein of unknown function whose sequence was previously demonstrated to contain a putative carbohydrate-binding domain.</p></sec><sec><title>Results</title><p>We here show that At5g39790 is chloroplast-localized, and binds starch, with a preference for amylose. The protein persists in starch binding under conditions of pH, redox and Mg<sup>+2 </sup>concentrations characteristic of both the day and night chloroplast cycles. Bioinformatic analysis demonstrates a diurnal pattern of gene expression, with an accumulation of transcript during the light cycle and decline during the dark cycle. A corresponding diurnal pattern of change in protein levels in leaves is also observed. Sequence analysis shows that At5g39790 has a strongly-predicted coiled-coil domain. Similar analysis of the set of starch metabolic enzymes shows that several have strong to moderate coiled-coil potential. Gene expression analysis shows strongly correlated patterns of co-expression between At5g39790 and several starch metabolic enzymes.</p></sec><sec><title>Conclusion</title><p>We propose that At5g39790 is a regulatory scaffold protein, persistently binding the starch granule, where it is positioned to interact by its coiled-coil domain with several potential starch metabolic enzyme binding-partners.</p></sec></abstract></article-meta></front></pmc><affiliations><list><country><li>Canada</li></country><region><li>Alberta</li></region><settlement><li>Calgary</li></settlement><orgName><li>Université de Calgary</li></orgName></list><tree><country name="Canada"><region name="Alberta"><name sortKey="Lohmeier Vogel, Elke M" sort="Lohmeier Vogel, Elke M" uniqKey="Lohmeier Vogel E" first="Elke M" last="Lohmeier-Vogel">Elke M. Lohmeier-Vogel</name></region><name sortKey="Kerk, David" sort="Kerk, David" uniqKey="Kerk D" first="David" last="Kerk">David Kerk</name><name sortKey="Moorhead, Greg Bg" sort="Moorhead, Greg Bg" uniqKey="Moorhead G" first="Greg Bg" last="Moorhead">Greg Bg Moorhead</name><name sortKey="Muench, Douglas G" sort="Muench, Douglas G" uniqKey="Muench D" first="Douglas G" last="Muench">Douglas G. Muench</name><name sortKey="Nimick, Mhairi" sort="Nimick, Mhairi" uniqKey="Nimick M" first="Mhairi" last="Nimick">Mhairi Nimick</name><name sortKey="Vickerman, Lori" sort="Vickerman, Lori" uniqKey="Vickerman L" first="Lori" last="Vickerman">Lori Vickerman</name><name sortKey="Wrobel, Susan" sort="Wrobel, Susan" uniqKey="Wrobel S" first="Susan" last="Wrobel">Susan Wrobel</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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